Membrane Fusion Intermediates via Directional and Full Assembly of the SNARE Complex

被引:178
|
作者
Hernandez, Javier M. [1 ]
Stein, Alexander [1 ]
Behrmann, Elmar [4 ]
Riedel, Dietmar [1 ]
Cypionka, Anna [1 ,2 ]
Farsi, Zohreh [1 ]
Walla, Peter J. [2 ,3 ]
Raunser, Stefan [4 ]
Jahn, Reinhard [1 ]
机构
[1] Max Planck Inst Biophys Chem, Dept Neurobiol, D-37077 Gottingen, Germany
[2] Max Planck Inst Biophys Chem, AG Biomol Spect & Single Mol Detect, D-37077 Gottingen, Germany
[3] Tech Univ Carolo Wilhelmina Braunschweig, Inst Phys & Theoret Chem, Dept Biophys Chem, D-38106 Braunschweig, Germany
[4] Max Planck Inst Mol Physiol, Dept Phys Biochem, D-44227 Dortmund, Germany
基金
美国国家卫生研究院;
关键词
HEMIFUSION; EXOCYTOSIS; PROMOTES; VISUALIZATION; SYNAPTOTAGMIN; MECHANISMS; RESOLUTION; RELEASE; DOCKING; LIPIDS;
D O I
10.1126/science.1221976
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Cellular membrane fusion is thought to proceed through intermediates including docking of apposed lipid bilayers, merging of proximal leaflets to form a hemifusion diaphragm, and fusion pore opening. A membrane-bridging four-helix complex of soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs) mediates fusion. However, how assembly of the SNARE complex generates docking and other fusion intermediates is unknown. Using a cell-free reaction, we identified intermediates visually and then arrested the SNARE fusion machinery when fusion was about to begin. Partial and directional assembly of SNAREs tightly docked bilayers, but efficient fusion and an extended form of hemifusion required assembly beyond the core complex to the membrane-connecting linkers. We propose that straining of lipids at the edges of an extended docking zone initiates fusion.
引用
收藏
页码:1581 / 1584
页数:4
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